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Volumn 14, Issue 3, 2013, Pages 282-294

A Proline-Tyrosine nuclear localization signal (PY-NLS) is required for the nuclear import of fission yeast PAB2, but not of human PABPN1

Author keywords

Kap104; Karyopherin; Pab2; PABPN1; PY NLS; S. pombe

Indexed keywords

ARGININE; BINDING PROTEIN; KARYOPHERIN; KARYOPHERIN BETA2; PAB2 PROTEIN; PABPN1 PROTEIN; PROTEIN; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 84873424140     PISSN: 13989219     EISSN: 16000854     Source Type: Journal    
DOI: 10.1111/tra.12036     Document Type: Article
Times cited : (20)

References (37)
  • 1
    • 69249222891 scopus 로고    scopus 로고
    • Nuclear localization signals and human disease
    • McLane LM, Corbett AH. Nuclear localization signals and human disease. IUBMB Life 2009;61:697-706.
    • (2009) IUBMB Life , vol.61 , pp. 697-706
    • McLane, L.M.1    Corbett, A.H.2
  • 3
    • 34247135913 scopus 로고    scopus 로고
    • Classical nuclear localization signals: definition, function, and interaction with importin alpha
    • Lange A, Mills RE, Lange CJ, Stewart M, Devine SE, Corbett AH. Classical nuclear localization signals: definition, function, and interaction with importin alpha. J Biol Chem 2007;282:5101-5105.
    • (2007) J Biol Chem , vol.282 , pp. 5101-5105
    • Lange, A.1    Mills, R.E.2    Lange, C.J.3    Stewart, M.4    Devine, S.E.5    Corbett, A.H.6
  • 4
    • 45149113882 scopus 로고    scopus 로고
    • A PY-NLS nuclear targeting signal is required for nuclear localization and function of the Saccharomyces cerevisiae mRNA-binding protein Hrp1
    • Lange A, Mills RE, Devine SE, Corbett AH. A PY-NLS nuclear targeting signal is required for nuclear localization and function of the Saccharomyces cerevisiae mRNA-binding protein Hrp1. J Biol Chem 2008;283:12926-12934.
    • (2008) J Biol Chem , vol.283 , pp. 12926-12934
    • Lange, A.1    Mills, R.E.2    Devine, S.E.3    Corbett, A.H.4
  • 6
    • 79960907910 scopus 로고    scopus 로고
    • The MAPK cascades: signaling components, nuclear roles and mechanisms of nuclear translocation
    • Plotnikov A, Zehorai E, Procaccia S, Seger R. The MAPK cascades: signaling components, nuclear roles and mechanisms of nuclear translocation. Biochim Biophys Acta 2011;1813:1619-1633.
    • (2011) Biochim Biophys Acta , vol.1813 , pp. 1619-1633
    • Plotnikov, A.1    Zehorai, E.2    Procaccia, S.3    Seger, R.4
  • 8
    • 78649650714 scopus 로고    scopus 로고
    • Recognition of nuclear targeting signals by Karyopherin-beta proteins
    • Xu D, Farmer A, Chook YM. Recognition of nuclear targeting signals by Karyopherin-beta proteins. Curr Opin Struct Biol 2010;20:782-790.
    • (2010) Curr Opin Struct Biol , vol.20 , pp. 782-790
    • Xu, D.1    Farmer, A.2    Chook, Y.M.3
  • 9
    • 79960912049 scopus 로고    scopus 로고
    • Nuclear import by karyopherin-betas: recognition and inhibition
    • Chook YM, Suel KE. Nuclear import by karyopherin-betas: recognition and inhibition. Biochim Biophys Acta 2011;1813:1593-1606.
    • (2011) Biochim Biophys Acta , vol.1813 , pp. 1593-1606
    • Chook, Y.M.1    Suel, K.E.2
  • 10
    • 33746776838 scopus 로고    scopus 로고
    • Rules for nuclear localization sequence recognition by karyopherin beta 2
    • Lee BJ, Cansizoglu AE, Suel KE, Louis TH, Zhang Z, Chook YM. Rules for nuclear localization sequence recognition by karyopherin beta 2. Cell 2006;126:543-558.
    • (2006) Cell , vol.126 , pp. 543-558
    • Lee, B.J.1    Cansizoglu, A.E.2    Suel, K.E.3    Louis, T.H.4    Zhang, Z.5    Chook, Y.M.6
  • 11
    • 2442482777 scopus 로고    scopus 로고
    • Structure and function of poly(A) binding proteins
    • Kuhn U, Wahle E. Structure and function of poly(A) binding proteins. Biochim Biophys Acta 2004;1678:67-84.
    • (2004) Biochim Biophys Acta , vol.1678 , pp. 67-84
    • Kuhn, U.1    Wahle, E.2
  • 12
    • 34147145820 scopus 로고    scopus 로고
    • Regulation of the nuclear poly(A)-binding protein by arginine methylation in fission yeast
    • Perreault A, Lemieux C, Bachand F. Regulation of the nuclear poly(A)-binding protein by arginine methylation in fission yeast. J Biol Chem 2007;282:7552-7562.
    • (2007) J Biol Chem , vol.282 , pp. 7552-7562
    • Perreault, A.1    Lemieux, C.2    Bachand, F.3
  • 13
    • 0039374447 scopus 로고    scopus 로고
    • Unusual sites of arginine methylation in Poly(A)-binding protein II and in vitro methylation by protein arginine methyltransferases PRMT1 and PRMT3
    • Smith JJ, Rucknagel KP, Schierhorn A, Tang J, Nemeth A, Linder M, Herschman HR, Wahle E. Unusual sites of arginine methylation in Poly(A)-binding protein II and in vitro methylation by protein arginine methyltransferases PRMT1 and PRMT3. J Biol Chem 1999;274:13229-13234.
    • (1999) J Biol Chem , vol.274 , pp. 13229-13234
    • Smith, J.J.1    Rucknagel, K.P.2    Schierhorn, A.3    Tang, J.4    Nemeth, A.5    Linder, M.6    Herschman, H.R.7    Wahle, E.8
  • 14
    • 69249151288 scopus 로고    scopus 로고
    • Poly(A) tail length is controlled by the nuclear poly(A)-binding protein regulating the interaction between poly(A) polymerase and the cleavage and polyadenylation specificity factor
    • Kuhn U, Gundel M, Knoth A, Kerwitz Y, Rudel S, Wahle E. Poly(A) tail length is controlled by the nuclear poly(A)-binding protein regulating the interaction between poly(A) polymerase and the cleavage and polyadenylation specificity factor. J Biol Chem 2009;284:22803-22814.
    • (2009) J Biol Chem , vol.284 , pp. 22803-22814
    • Kuhn, U.1    Gundel, M.2    Knoth, A.3    Kerwitz, Y.4    Rudel, S.5    Wahle, E.6
  • 16
    • 0034698136 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae RNA-binding protein Rbp29 functions in cytoplasmic mRNA metabolism
    • Winstall E, Sadowski M, Kuhn U, Wahle E, Sachs AB. The Saccharomyces cerevisiae RNA-binding protein Rbp29 functions in cytoplasmic mRNA metabolism. J Biol Chem 2000;275:21817-21826.
    • (2000) J Biol Chem , vol.275 , pp. 21817-21826
    • Winstall, E.1    Sadowski, M.2    Kuhn, U.3    Wahle, E.4    Sachs, A.B.5
  • 17
    • 73649112807 scopus 로고    scopus 로고
    • The nuclear poly(A)-binding protein interacts with the exosome to promote synthesis of noncoding small nucleolar RNAs
    • Lemay JF, D'Amours A, Lemieux C, Lackner DH, St-Sauveur VG, Bahler J, Bachand F. The nuclear poly(A)-binding protein interacts with the exosome to promote synthesis of noncoding small nucleolar RNAs. Mol Cell 2010;37:34-45.
    • (2010) Mol Cell , vol.37 , pp. 34-45
    • Lemay, J.F.1    D'Amours, A.2    Lemieux, C.3    Lackner, D.H.4    St-Sauveur, V.G.5    Bahler, J.6    Bachand, F.7
  • 18
    • 80053597137 scopus 로고    scopus 로고
    • A Pre-mRNA degradation pathway that selectively targets intron-containing genes requires the nuclear poly(A)-binding protein
    • Lemieux C, Marguerat S, Lafontaine J, Barbezier N, Bahler J, Bachand F. A Pre-mRNA degradation pathway that selectively targets intron-containing genes requires the nuclear poly(A)-binding protein. Mol Cell 2011;44:108-119.
    • (2011) Mol Cell , vol.44 , pp. 108-119
    • Lemieux, C.1    Marguerat, S.2    Lafontaine, J.3    Barbezier, N.4    Bahler, J.5    Bachand, F.6
  • 19
    • 85011942156 scopus 로고    scopus 로고
    • Crossing the borders: poly(A)-binding proteins working on both sides of the fence
    • Lemay JF, Lemieux C, St-Andre O, Bachand F. Crossing the borders: poly(A)-binding proteins working on both sides of the fence. RNA Biol 2010;7:291-295.
    • (2010) RNA Biol , vol.7 , pp. 291-295
    • Lemay, J.F.1    Lemieux, C.2    St-Andre, O.3    Bachand, F.4
  • 20
    • 0033951076 scopus 로고    scopus 로고
    • Deciphering the cellular pathway for transport of poly(A)-binding protein II
    • Calado A, Kutay U, Kuhn U, Wahle E, Carmo-Fonseca M. Deciphering the cellular pathway for transport of poly(A)-binding protein II. RNA 2000;6:245-256.
    • (2000) RNA , vol.6 , pp. 245-256
    • Calado, A.1    Kutay, U.2    Kuhn, U.3    Wahle, E.4    Carmo-Fonseca, M.5
  • 21
    • 67249129775 scopus 로고    scopus 로고
    • Cotranscriptional recruitment of the nuclear poly(A)-binding protein Pab2 to nascent transcripts and association with translating mRNPs
    • Lemieux C, Bachand F. Cotranscriptional recruitment of the nuclear poly(A)-binding protein Pab2 to nascent transcripts and association with translating mRNPs. Nucleic Acids Res 2009;37:3418-3430.
    • (2009) Nucleic Acids Res , vol.37 , pp. 3418-3430
    • Lemieux, C.1    Bachand, F.2
  • 22
    • 80053046235 scopus 로고    scopus 로고
    • Arginine methylation of the nuclear poly(a) binding protein weakens the interaction with its nuclear import receptor, transportin
    • Fronz K, Guttinger S, Burkert K, Kuhn U, Stohr N, Schierhorn A, Wahle E. Arginine methylation of the nuclear poly(a) binding protein weakens the interaction with its nuclear import receptor, transportin. J Biol Chem 2011;286:32986-32994.
    • (2011) J Biol Chem , vol.286 , pp. 32986-32994
    • Fronz, K.1    Guttinger, S.2    Burkert, K.3    Kuhn, U.4    Stohr, N.5    Schierhorn, A.6    Wahle, E.7
  • 23
    • 45849096845 scopus 로고    scopus 로고
    • Modular organization and combinatorial energetics of proline-tyrosine nuclear localization signals
    • Suel KE, Gu H, Chook YM. Modular organization and combinatorial energetics of proline-tyrosine nuclear localization signals. PLoS Biol 2008;6:e137.
    • (2008) PLoS Biol , vol.6
    • Suel, K.E.1    Gu, H.2    Chook, Y.M.3
  • 24
    • 2442642905 scopus 로고    scopus 로고
    • Identification of genes encoding putative nucleoporins and transport factors in the fission yeast Schizosaccharomyces pombe: a deletion analysis
    • Chen XQ, Du X, Liu J, Balasubramanian MK, Balasundaram D. Identification of genes encoding putative nucleoporins and transport factors in the fission yeast Schizosaccharomyces pombe: a deletion analysis. Yeast 2004;21:495-509.
    • (2004) Yeast , vol.21 , pp. 495-509
    • Chen, X.Q.1    Du, X.2    Liu, J.3    Balasubramanian, M.K.4    Balasundaram, D.5
  • 25
    • 0036811144 scopus 로고    scopus 로고
    • The sal3(+) gene encodes an importin-beta implicated in the nuclear import of Cdc25 in Schizosaccharomyces pombe
    • Chua G, Lingner C, Frazer C, Young PG. The sal3(+) gene encodes an importin-beta implicated in the nuclear import of Cdc25 in Schizosaccharomyces pombe. Genetics 2002;162:689-703.
    • (2002) Genetics , vol.162 , pp. 689-703
    • Chua, G.1    Lingner, C.2    Frazer, C.3    Young, P.G.4
  • 26
    • 84862825917 scopus 로고    scopus 로고
    • The karyopherin Sal3 is required for nuclear import of the core RNA interference pathway protein Rdp1
    • doi:10.1111/j.1600-0854.2012.01333.x.
    • Park J, Freitag SI, Young PG, Hobman TC. The karyopherin Sal3 is required for nuclear import of the core RNA interference pathway protein Rdp1. Traffic 2012. doi:10.1111/j.1600-0854.2012.01333.x.
    • (2012) Traffic
    • Park, J.1    Freitag, S.I.2    Young, P.G.3    Hobman, T.C.4
  • 28
    • 0028318159 scopus 로고
    • Leptomycin B targets a regulatory cascade of crm1, a fission yeast nuclear protein, involved in control of higher order chromosome structure and gene expression
    • Nishi K, Yoshida M, Fujiwara D, Nishikawa M, Horinouchi S, Beppu T. Leptomycin B targets a regulatory cascade of crm1, a fission yeast nuclear protein, involved in control of higher order chromosome structure and gene expression. J Biol Chem 1994;269:6320-6324.
    • (1994) J Biol Chem , vol.269 , pp. 6320-6324
    • Nishi, K.1    Yoshida, M.2    Fujiwara, D.3    Nishikawa, M.4    Horinouchi, S.5    Beppu, T.6
  • 30
    • 67650136746 scopus 로고    scopus 로고
    • Kap104p imports the PY-NLS-containing transcription factor Tfg2p into the nucleus
    • Suel KE, Chook YM. Kap104p imports the PY-NLS-containing transcription factor Tfg2p into the nucleus. J Biol Chem 2009;284:15416-15424.
    • (2009) J Biol Chem , vol.284 , pp. 15416-15424
    • Suel, K.E.1    Chook, Y.M.2
  • 32
    • 82655189968 scopus 로고    scopus 로고
    • Evolutionary development of redundant nuclear localization signals in the mRNA export factor NXF1
    • Zhang ZC, Satterly N, Fontoura BM, Chook YM. Evolutionary development of redundant nuclear localization signals in the mRNA export factor NXF1. Mol Biol Cell 2011;22:4657-4668.
    • (2011) Mol Biol Cell , vol.22 , pp. 4657-4668
    • Zhang, Z.C.1    Satterly, N.2    Fontoura, B.M.3    Chook, Y.M.4
  • 34
    • 32944469753 scopus 로고    scopus 로고
    • Copper induces cytoplasmic retention of fission yeast transcription factor cuf1
    • Beaudoin J, Labbe S. Copper induces cytoplasmic retention of fission yeast transcription factor cuf1. Eukaryot Cell 2006;5:277-292.
    • (2006) Eukaryot Cell , vol.5 , pp. 277-292
    • Beaudoin, J.1    Labbe, S.2
  • 35
    • 34249746266 scopus 로고    scopus 로고
    • Crm1-mediated nuclear export of the Schizosaccharomyces pombe transcription factor Cuf1 during a shift from low to high copper concentrations
    • Beaudoin J, Labbe S. Crm1-mediated nuclear export of the Schizosaccharomyces pombe transcription factor Cuf1 during a shift from low to high copper concentrations. Eukaryot Cell 2007;6:764-775.
    • (2007) Eukaryot Cell , vol.6 , pp. 764-775
    • Beaudoin, J.1    Labbe, S.2
  • 36
    • 0035504113 scopus 로고    scopus 로고
    • Oligomerization of polyalanine expanded PABPN1 facilitates nuclear protein aggregation that is associated with cell death
    • Fan X, Dion P, Laganiere J, Brais B, Rouleau GA. Oligomerization of polyalanine expanded PABPN1 facilitates nuclear protein aggregation that is associated with cell death. Hum Mol Genet 2001;10:2341-2351.
    • (2001) Hum Mol Genet , vol.10 , pp. 2341-2351
    • Fan, X.1    Dion, P.2    Laganiere, J.3    Brais, B.4    Rouleau, G.A.5
  • 37
    • 67649359948 scopus 로고    scopus 로고
    • A methyltransferase-independent function for Rmt3 in ribosomal subunit homeostasis
    • Perreault A, Gascon S, D'Amours A, Aletta JM, Bachand F. A methyltransferase-independent function for Rmt3 in ribosomal subunit homeostasis. J Biol Chem 2009;284:15026-15037.
    • (2009) J Biol Chem , vol.284 , pp. 15026-15037
    • Perreault, A.1    Gascon, S.2    D'Amours, A.3    Aletta, J.M.4    Bachand, F.5


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